We have seen that amino acid residues Asp52 and Glu35 are required for lysozyme?s catalytic activity:...
We have seen that amino acid residues Asp52 and Glu35 are required for lysozyme?s catalytic activity:
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• Assume that the side chain pKas are the usual valuesof 3.90 for Asp and 4.07 for Glu. At pH 5.0 (the pH optimum for lysozyme) what proportion of enzyme molecules have both Asp52 and Glu35 in the correct ionization state?
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• Are the pKa values likely to be correct? What change in pKa might be present within lysozyme?
Homework Answers
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We have seen that amino acid residues Asp52 and Glu35 are
required for lysozyme?s catalytic activity:...
The active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and Asp52....
The active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and Asp52. The pKa values of the carboxyl side chains of these residues are 5.9 and 4.5, respectively. What is the ionization state (protonated or deprotonated) of each residue at pH 5.2, the pH optimum of lysozyme? How can the ionization states of these residues explain the pH-activity profile of lysozyme.
7. Lysozyme has two key catalytic residues, Glu 35 with a pKa of 5.9 and Asp...
7. Lysozyme has two key catalytic residues, Glu 35 with a pKa of 5.9 and Asp 52 with a pKa of 4.5. If the pH optimum for this enzyme is 5.0, what does this tell you about the mechanism? a. Glu 35 acts more likely a general acid than Asp 52. b. Glu 35 acts more likely a general base than Asp 52. c. Asp 52 acts more likely a general acid than Glu 35. d. None of the above...
Due to the interactions with other amino acids in the protein, the pKa of Glu35 and...
Due to the interactions with other
amino acids in the protein, the pKa of Glu35 and Asp 52
are both shifted from the standard values found in our
table. The actual pKa values are 5.9 for
Glu35 and 4.5 for Asp52 respectively. Using these pKa values, and
the H-H equation, calculate the ratio of deprotonated to protonated
side chains for both Glu35 and Asp59 at pH 4.0, pH 5.2 and pH 6.0
(six total calculations). Using your
calculations, clearly explain why the...
24. The enzymatic activity of lysozyme is optimal at pH S.2 and decreases above and below...
24. The enzymatic activity of lysozyme is optimal at pH S.2 and decreases above and below this phH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu and Asp5?. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5, respectively. What is the ionization state of each residue at the pH optimum of lysozyme? (1 Pt) a. vcan the ionization states of these two amino acid residues explain...
Suppose you are researching a special enzyme named "Generic Enzyme." Generic Enzyme has an amino acid...
Suppose you are researching a special enzyme named "Generic Enzyme." Generic Enzyme has an amino acid side chain functional group that must be in the protonated form for the enzyme to be active. You have just purified Generic Enzyme and found that 1 in every 4 individual Generic Enzyme molecules is active. Your special Generic Enzyme is at a pH of 7.75. Generic enzyme has a phenolic hydroxyl group which is responsible for its catalytic activity. What is the pKa...
10) Would an amino acid with the given side chain be most likely found in the hydrophobic or hydrophilic region of a pr...
10) Would an amino acid with the given side chain be most likely found in the hydrophobic or hydrophilic region of a protein? -CH-CH3 он CH2-CH-CH3 он CH3 11) What process occurs when heat, acids, bases, and heavy metal ions cause loss of biological function of a protein? 12) Answer the following questions regarding enzyme activity: a) The optimum temperature and pH for most biological enzymes is b) The molecules to which an enzyme binds are called the c) The...
questions e-f and g.and k. a) Use the 3 letter symbols for a 6 amino acid...
questions e-f and g.and k.
a) Use the 3 letter symbols for a 6 amino acid peptide chain containing at least one polar and at least one acidic or basic amino acid. (All at physiological pH.) Asp - Gly-Glu-Tyr- Phe- Ala OM b) Draw the primary structure with its peptide bonds, side chains, etc. in the correct order. CH3 NH - E-N -CH. - CH - C- 2-I U=0 -ch- & N-chi- CH₃ CH ₂ Coo CH н My Coo...
5. D-sorbital is found in 'sugar-free' chewing gum. It is formed by reducing D-glucose with NaBH Draw the structure of D-sorbital. s. (4 pts) Classify the following amino acid as polar, n...
5. D-sorbital is found in 'sugar-free' chewing gum. It is formed by reducing D-glucose with NaBH Draw the structure of D-sorbital. s. (4 pts) Classify the following amino acid as polar, non- polar, acidic, or basic: 6 (4 pts) The amino acid threonine (thr) has two chiral carbons. Draw a Fischer projection of the 2S,3S configuration of threonine. キ 7.(11 pts) Draw the tripeptide lys-asp-ser at physiological pH 8. (8 pts) The pK, values for aspartic acid are 2.10, 9.82...
11 Department of Biological Sciences BIOCHEMISTRY Test 2.2018 H. Nucleic Acid, Sequencing of DNA: Amino Acids...
11 Department of Biological Sciences BIOCHEMISTRY Test 2.2018 H. Nucleic Acid, Sequencing of DNA: Amino Acids Hydrolysis of salt Laboratory buffers, Polyprotie acids QUESTIONS 1. The DNA strand complementary to the strand 3-GTAGCGTAT-Y' would have the sequence a SLTACOCATAT-3 b.3.CATOXICATA-S c. 3-ATGCGTATA-S" ATATGCGTAS 2. When cytosine is treated with bisulfite, the amino group is replaced with a carbonyl group. Identify the resulting base a. adenine b. guanine c uracil d. thyminee. typoxanthine 3. How many amino acids would be in...
Cyw Ala Ατα Ile Ausn Lou Asp aly Lys Ser Which molecule below is asubunit of...
Cyw Ala Ατα Ile Ausn Lou Asp aly Lys Ser Which molecule below is asubunit of peptide chains a. Acetic acid b. Alanine O. ATP d. Gracil Report the charge on most aqueous aspartie acid molecules at pH-7. Report the approximate p values for the amino acid whose titration curve is shown below (note there may be more slots for answer than answers). A) Value 1 B) Value 2 c) Value 3 c) Value 4 The structure of a rare...
7. Lysozyme has two key catalytic residues, Glu 35 with a pKa of 5.9 and Asp 52 with a pKa of 4.5. If the pH optimum for this enzyme is 5.0, what does this tell you about the mechanism? a. Glu 35 acts more likely a general acid than Asp 52. b. Glu 35 acts more likely a general base than Asp 52. c. Asp 52 acts more likely a general acid than Glu 35. d. None of the above...
Due to the interactions with other
amino acids in the protein, the pKa of Glu35 and Asp 52
are both shifted from the standard values found in our
table. The actual pKa values are 5.9 for
Glu35 and 4.5 for Asp52 respectively. Using these pKa values, and
the H-H equation, calculate the ratio of deprotonated to protonated
side chains for both Glu35 and Asp59 at pH 4.0, pH 5.2 and pH 6.0
(six total calculations). Using your
calculations, clearly explain why the...
24. The enzymatic activity of lysozyme is optimal at pH S.2 and decreases above and below this phH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu and Asp5?. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5, respectively. What is the ionization state of each residue at the pH optimum of lysozyme? (1 Pt) a. vcan the ionization states of these two amino acid residues explain...
10) Would an amino acid with the given side chain be most likely found in the hydrophobic or hydrophilic region of a protein? -CH-CH3 он CH2-CH-CH3 он CH3 11) What process occurs when heat, acids, bases, and heavy metal ions cause loss of biological function of a protein? 12) Answer the following questions regarding enzyme activity: a) The optimum temperature and pH for most biological enzymes is b) The molecules to which an enzyme binds are called the c) The...
questions e-f and g.and k.
a) Use the 3 letter symbols for a 6 amino acid peptide chain containing at least one polar and at least one acidic or basic amino acid. (All at physiological pH.) Asp - Gly-Glu-Tyr- Phe- Ala OM b) Draw the primary structure with its peptide bonds, side chains, etc. in the correct order. CH3 NH - E-N -CH. - CH - C- 2-I U=0 -ch- & N-chi- CH₃ CH ₂ Coo CH н My Coo...
5. D-sorbital is found in 'sugar-free' chewing gum. It is formed by reducing D-glucose with NaBH Draw the structure of D-sorbital. s. (4 pts) Classify the following amino acid as polar, non- polar, acidic, or basic: 6 (4 pts) The amino acid threonine (thr) has two chiral carbons. Draw a Fischer projection of the 2S,3S configuration of threonine. キ 7.(11 pts) Draw the tripeptide lys-asp-ser at physiological pH 8. (8 pts) The pK, values for aspartic acid are 2.10, 9.82...
11 Department of Biological Sciences BIOCHEMISTRY Test 2.2018 H. Nucleic Acid, Sequencing of DNA: Amino Acids Hydrolysis of salt Laboratory buffers, Polyprotie acids QUESTIONS 1. The DNA strand complementary to the strand 3-GTAGCGTAT-Y' would have the sequence a SLTACOCATAT-3 b.3.CATOXICATA-S c. 3-ATGCGTATA-S" ATATGCGTAS 2. When cytosine is treated with bisulfite, the amino group is replaced with a carbonyl group. Identify the resulting base a. adenine b. guanine c uracil d. thyminee. typoxanthine 3. How many amino acids would be in...
Cyw Ala Ατα Ile Ausn Lou Asp aly Lys Ser Which molecule below is asubunit of peptide chains a. Acetic acid b. Alanine O. ATP d. Gracil Report the charge on most aqueous aspartie acid molecules at pH-7. Report the approximate p values for the amino acid whose titration curve is shown below (note there may be more slots for answer than answers). A) Value 1 B) Value 2 c) Value 3 c) Value 4 The structure of a rare...
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